Profiling the Distribution of N-Glycosylation in Therapeutic Antibodies

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Immunoglobulin G molecules have become attractive as targeted therapeutic proteins, due to their high specificity and long circulation time. Glycosylation patterns determine the stability and bio-disposition of these recombinant protein drugs in vivo, as well as the efficacy, folding, binding affinity, specificity and pharmacokinetic properties. Therefore, a complete characterization of the biotherapeutic IgG glycosylation is desirable.

In this study, we demonstrated how a comprehensive MS/MS analysis of the glycopeptides can be achieved by targeting the known nature of the glycosylation structures.

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